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Protein

Receptor of activated protein C kinase 1

Gene

RACK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158).21 Publications
(Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells.1 Publication
(Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs.1 Publication
(Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs.1 Publication
(Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • cyclin binding Source: UniProtKB
  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • enzyme binding Source: BHF-UCL
  • ion channel inhibitor activity Source: UniProtKB
  • protein-containing complex scaffold activity Source: BHF-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein kinase C binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein tyrosine kinase inhibitor activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • SH2 domain binding Source: UniProtKB
  • signaling adaptor activity Source: ParkinsonsUK-UCL
  • signaling receptor binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Ribonucleoprotein, Ribosomal protein
Biological processApoptosis, Biological rhythms, Cell cycle, Gastrulation, Growth regulation, Host-virus interaction, Translation regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5626978 TNFR1-mediated ceramide production

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P63244

SIGNOR Signaling Network Open Resource

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SIGNORi
P63244

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Receptor of activated protein C kinase 1
Alternative name(s):
Cell proliferation-inducing gene 21 protein
Guanine nucleotide-binding protein subunit beta-2-like 1
Guanine nucleotide-binding protein subunit beta-like protein 12.3
Human lung cancer oncogene 7 protein
Short name:
HLC-7
Receptor for activated C kinase
Small ribosomal subunit protein RACK11 Publication
Cleaved into the following chain:
Alternative name(s):
Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RACK1Imported
Synonyms:GNB2L1
ORF Names:HLC7, PIG21
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000204628.11

Human Gene Nomenclature Database

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HGNCi
HGNC:4399 RACK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
176981 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P63244

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi36 – 38RDK → DDE in DEmut; abolishes association with the ribosome and ability to initiate the ribosome quality control (RQC). 1 Publication3
Mutagenesisi52Y → F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation. 3 Publications1
Mutagenesisi57R → A: Decreased binding to PTK2/FAK1; when associated with A-60. 1 Publication1
Mutagenesisi60R → A: Decreased binding to PTK2/FAK1; when associated with A-57. 1 Publication1
Mutagenesisi127K → A: Decreased binding to PTK2/FAK1; when associated with A-130. 1 Publication1
Mutagenesisi130K → A: Decreased binding to PTK2/FAK1; when associated with A-127. 1 Publication1
Mutagenesisi140Y → F: No effect on binding to SRC. 2 Publications1
Mutagenesisi194Y → F: No effect on binding to SRC. 2 Publications1
Mutagenesisi228Y → F: No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-246 and F-302. 2 Publications1
Mutagenesisi246Y → F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302. 2 Publications1
Mutagenesisi276 – 279STSS → EEEE: Enhanced translation of mRNAs containing poly-A leaders. 1 Publication4
Mutagenesisi278S → E: Enhanced translation of mRNAs containing poly-A leaders. 1 Publication1
Mutagenesisi302Y → F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246. 2 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10399

Open Targets

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OpenTargetsi
ENSG00000204628

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28779

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
GNB2L1

Domain mapping of disease mutations (DMDM)

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DMDMi
54037168

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004244801 – 317Receptor of activated protein C kinase 1Add BLAST317
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources1 Publication
ChainiPRO_00001277312 – 317Receptor of activated protein C kinase 1, N-terminally processedAdd BLAST316

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylthreonine; in Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processedCombined sources1 Publication1
Modified residuei6PhosphothreonineCombined sources1
Modified residuei10PhosphothreonineCombined sources1
Modified residuei52Phosphotyrosine; by ABL11 Publication1
Modified residuei96PhosphothreonineCombined sources1
Modified residuei130N6-acetyllysineCombined sources1
Modified residuei183N6-acetyllysineBy similarity1
Modified residuei228Phosphotyrosine1 Publication1
Modified residuei276Phosphoserine; by viral VacV B1 kinaseCombined sources1 Publication1
Modified residuei277Phosphothreonine; by viral VacV B1 kinase1 Publication1
Modified residuei278Phosphoserine; by viral VacV B1 kinase1 Publication1
Modified residuei279Phosphoserine; by viral VacV B1 kinase1 Publication1
Modified residuei316PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.3 Publications
(Microbial infection) Phosphorylated by vaccinia virus B1 kinase on serine and threonine residues; this phosphorylation remodels the ribosome properties, favoring the viral mRNA translation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P63244

MaxQB - The MaxQuant DataBase

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MaxQBi
P63244

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P63244

PeptideAtlas

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PeptideAtlasi
P63244

PRoteomics IDEntifications database

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PRIDEi
P63244

ProteomicsDB human proteome resource

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ProteomicsDBi
57512

Consortium for Top Down Proteomics

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TopDownProteomicsi
P63244

2D gel databases

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00848226
P63244

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P63244

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P63244

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63244

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

In the liver, expressed at higher levels in activated hepatic stellate cells than in hepatocytes or Kupffer cells. Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor liver tissue.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000204628 Expressed in 246 organ(s), highest expression level in female gonad

CleanEx database of gene expression profiles

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CleanExi
HS_GNB2L1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63244 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63244 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004288
HPA021676

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer; also forms homodimers and homooligomers (PubMed:20529362, PubMed:15140893). Interacts with CPNE3 (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component of the small (40S) ribosomal subunit (By similarity). Interacts with the 80S ribosome (PubMed:23636399). Binds SLC9A3R1. Forms a ternary complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of RACK1. Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA. Interacts with AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation. Interacts with RHOA; this enhances RHOA activation and promotes cell migration. Interacts with CHRM2; the interaction regulates CHRM2 internalization. Interacts with TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with LARP4B. Interacts with LARP4 (PubMed:21098120). Interacts with PKD2L1.By similarity28 Publications
(Microbial infection) Interacts with Y.pseudotuberculosis yopK.1 Publication
(Microbial infection) Interacts with Y.pseudotuberculosis yopK. Interacts with a number of viral proteins including Epstein-Barr virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef phosphorylation by PKC.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115671, 223 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P63244

Database of interacting proteins

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DIPi
DIP-46736N

Protein interaction database and analysis system

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IntActi
P63244, 106 interactors

Molecular INTeraction database

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MINTi
P63244

STRING: functional protein association networks

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STRINGi
9606.ENSP00000426909

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1317
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P63244

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P63244

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati13 – 44WD 1Add BLAST32
Repeati61 – 91WD 2Add BLAST31
Repeati103 – 133WD 3Add BLAST31
Repeati146 – 178WD 4Add BLAST33
Repeati190 – 220WD 5Add BLAST31
Repeati231 – 260WD 6Add BLAST30
Repeati281 – 311WD 7Add BLAST31

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 7 WD repeats mediate protein-protein interactions with binding partners.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0279 Eukaryota
ENOG410XQGZ LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154461

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000277

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P63244

KEGG Orthology (KO)

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KOi
K14753

Identification of Orthologs from Complete Genome Data

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OMAi
CKAMLWD

Database for complete collections of gene phylogenies

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PhylomeDBi
P63244

TreeFam database of animal gene trees

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TreeFami
TF300600

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.130.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR020472 G-protein_beta_WD-40_rep
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00400 WD40, 7 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00320 GPROTEINBRPT

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00320 WD40, 7 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50978 SSF50978, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00678 WD_REPEATS_1, 4 hits
PS50082 WD_REPEATS_2, 6 hits
PS50294 WD_REPEATS_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 21 potential isoforms that are computationally mapped.Show allAlign All

P63244-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET
60 70 80 90 100
NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR
110 120 130 140 150
FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW
160 170 180 190 200
VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA NCKLKTNHIG HTGYLNTVTV
210 220 230 240 250
SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC FSPNRYWLCA
260 270 280 290 300
ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA
310
GYTDNLVRVW QVTIGTR
Length:317
Mass (Da):35,077
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i257F91E369ED2044
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 21 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RFX4D6RFX4_HUMAN
Receptor of-activated protein C kin...
RACK1
194Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6REE5D6REE5_HUMAN
Receptor of-activated protein C kin...
RACK1
321Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6R9L0D6R9L0_HUMAN
Receptor of-activated protein C kin...
RACK1
300Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y8W2H0Y8W2_HUMAN
Receptor of-activated protein C kin...
RACK1
274Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RAC2D6RAC2_HUMAN
Receptor of-activated protein C kin...
RACK1
269Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6R9Z1D6R9Z1_HUMAN
Receptor of-activated protein C kin...
RACK1
236Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YAM7H0YAM7_HUMAN
Receptor of-activated protein C kin...
RACK1
247Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y8R5H0Y8R5_HUMAN
Receptor of-activated protein C kin...
RACK1
138Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KPE3J3KPE3_HUMAN
Receptor of-activated protein C kin...
RACK1
273Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RHH4D6RHH4_HUMAN
Receptor of-activated protein C kin...
RACK1
233Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAO21313 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAR24619 differs from that shown. Reason: Frameshift at position 94.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti70 – 111Missing in BAG53102 (PubMed:14702039).CuratedAdd BLAST42
Sequence conflicti94T → TRK in AAR24619 (Ref. 3) Curated1
Sequence conflicti221L → F in BAD96208 (Ref. 6) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M24194 mRNA Translation: AAA59626.1
AY159316 mRNA Translation: AAO21313.1 Different initiation.
AY336089 mRNA Translation: AAR24619.1 Frameshift.
AK095666 mRNA Translation: BAG53102.1
CR456978 mRNA Translation: CAG33259.1
CR541909 mRNA Translation: CAG46707.1
AK222488 mRNA Translation: BAD96208.1
CH471165 Genomic DNA Translation: EAW53692.1
CH471165 Genomic DNA Translation: EAW53702.1
BC000214 mRNA Translation: AAH00214.1
BC000366 mRNA Translation: AAH00366.1
BC010119 mRNA Translation: AAH10119.1
BC014256 mRNA Translation: AAH14256.1
BC014788 mRNA Translation: AAH14788.1
BC017287 mRNA Translation: AAH17287.1
BC019093 mRNA Translation: AAH19093.1
BC019362 mRNA Translation: AAH19362.1
BC021993 mRNA Translation: AAH21993.1
BC032006 mRNA Translation: AAH32006.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34324.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B33928

NCBI Reference Sequences

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RefSeqi
NP_006089.1, NM_006098.4

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.5662

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000512805; ENSP00000426909; ENSG00000204628

Database of genes from NCBI RefSeq genomes

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GeneIDi
10399

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10399

UCSC genome browser

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UCSCi
uc003mni.2 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24194 mRNA Translation: AAA59626.1
AY159316 mRNA Translation: AAO21313.1 Different initiation.
AY336089 mRNA Translation: AAR24619.1 Frameshift.
AK095666 mRNA Translation: BAG53102.1
CR456978 mRNA Translation: CAG33259.1
CR541909 mRNA Translation: CAG46707.1
AK222488 mRNA Translation: BAD96208.1
CH471165 Genomic DNA Translation: EAW53692.1
CH471165 Genomic DNA Translation: EAW53702.1
BC000214 mRNA Translation: AAH00214.1
BC000366 mRNA Translation: AAH00366.1
BC010119 mRNA Translation: AAH10119.1
BC014256 mRNA Translation: AAH14256.1
BC014788 mRNA Translation: AAH14788.1
BC017287 mRNA Translation: AAH17287.1
BC019093 mRNA Translation: AAH19093.1
BC019362 mRNA Translation: AAH19362.1
BC021993 mRNA Translation: AAH21993.1
BC032006 mRNA Translation: AAH32006.1
CCDSiCCDS34324.1
PIRiB33928
RefSeqiNP_006089.1, NM_006098.4
UniGeneiHs.5662

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AOWX-ray2.45A/B/C1-317[»]
4UG0electron microscopy-Sg1-317[»]
4V6Xelectron microscopy5.00Ag1-317[»]
5A2Qelectron microscopy3.90g1-315[»]
5AJ0electron microscopy3.50Bg1-317[»]
5FLXelectron microscopy3.90g1-317[»]
5LKSelectron microscopy3.60Sg1-317[»]
5OA3electron microscopy4.30g1-315[»]
5T2Celectron microscopy3.60AI1-317[»]
5VYCX-ray6.00g1/g2/g3/g4/g5/g61-317[»]
6EK0electron microscopy2.90Sg1-317[»]
6FECelectron microscopy6.30m2-314[»]
6G18electron microscopy3.60g1-317[»]
6G51electron microscopy4.10g1-317[»]
6G53electron microscopy4.50g1-317[»]
6G5Helectron microscopy3.60g1-317[»]
6G5Ielectron microscopy3.50g1-317[»]
ProteinModelPortaliP63244
SMRiP63244
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115671, 223 interactors
CORUMiP63244
DIPiDIP-46736N
IntActiP63244, 106 interactors
MINTiP63244
STRINGi9606.ENSP00000426909

PTM databases

iPTMnetiP63244
PhosphoSitePlusiP63244
SwissPalmiP63244

Polymorphism and mutation databases

BioMutaiGNB2L1
DMDMi54037168

2D gel databases

REPRODUCTION-2DPAGEiIPI00848226
P63244

Proteomic databases

EPDiP63244
MaxQBiP63244
PaxDbiP63244
PeptideAtlasiP63244
PRIDEiP63244
ProteomicsDBi57512
TopDownProteomicsiP63244

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10399
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000512805; ENSP00000426909; ENSG00000204628
GeneIDi10399
KEGGihsa:10399
UCSCiuc003mni.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10399
DisGeNETi10399
EuPathDBiHostDB:ENSG00000204628.11

GeneCards: human genes, protein and diseases

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GeneCardsi
RACK1
HGNCiHGNC:4399 RACK1
HPAiCAB004288
HPA021676
MIMi176981 gene
neXtProtiNX_P63244
OpenTargetsiENSG00000204628
PharmGKBiPA28779

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0279 Eukaryota
ENOG410XQGZ LUCA
GeneTreeiENSGT00940000154461
HOVERGENiHBG000277
InParanoidiP63244
KOiK14753
OMAiCKAMLWD
PhylomeDBiP63244
TreeFamiTF300600

Enzyme and pathway databases

ReactomeiR-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5626978 TNFR1-mediated ceramide production
SignaLinkiP63244
SIGNORiP63244

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RACK1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
GNB2L1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
10399

Protein Ontology

More...
PROi
PR:P63244

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000204628 Expressed in 246 organ(s), highest expression level in female gonad
CleanExiHS_GNB2L1
ExpressionAtlasiP63244 baseline and differential
GenevisibleiP63244 HS

Family and domain databases

Gene3Di2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR020472 G-protein_beta_WD-40_rep
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PfamiView protein in Pfam
PF00400 WD40, 7 hits
PRINTSiPR00320 GPROTEINBRPT
SMARTiView protein in SMART
SM00320 WD40, 7 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 4 hits
PS50082 WD_REPEATS_2, 6 hits
PS50294 WD_REPEATS_REGION, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRACK1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P63244
Secondary accession number(s): B3KTJ0
, D3DWS0, P25388, P99049, Q53HU2, Q5J8M6, Q5VLR4, Q6FH47
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 155 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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